MCA3_MOUSE
ID MCA3_MOUSE Reviewed; 174 AA.
AC Q9D1M4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Eukaryotic translation elongation factor 1 epsilon-1;
DE AltName: Full=Elongation factor p18;
DE AltName: Full=Multisynthase complex auxiliary component p18 {ECO:0000303|PubMed:12060739};
GN Name=Eef1e1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBUNIT.
RX PubMed=12060739; DOI=10.1073/pnas.122110199;
RA Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H., Ko Y.-G.,
RA Kim S.;
RT "p38 is essential for the assembly and stability of macromolecular tRNA
RT synthetase complex: implications for its physiological significance.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15680327; DOI=10.1016/j.cell.2004.11.054;
RA Park B.-J., Kang J.W., Lee S.W., Choi S.-J., Shin Y.K., Ahn Y.H.,
RA Choi Y.H., Choi D., Lee K.S., Kim S.;
RT "The haploinsufficient tumor suppressor p18 upregulates p53 via
RT interactions with ATM/ATR.";
RL Cell 120:209-221(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Positive modulator of ATM response to DNA damage.
CC {ECO:0000269|PubMed:15680327}.
CC -!- SUBUNIT: Part of a multisubunit complex that groups tRNA ligases for
CC Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys
CC (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1)
CC and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18
CC (PubMed:12060739). Can interact simultaneously with MARS1 and EPRS1.
CC Forms a linear complex that contains MARS1, EEF1E1, EPRS1 and AIMP2
CC that is at the core of the multisubunit complex. Interacts with ATM and
CC ATR. The interaction with ATM, which takes place independently of TP53,
CC is induced by DNA damage that may occur during genotoxic stress or cell
CC growth. The interaction with ATR is enhanced by UV irradiation (By
CC similarity). {ECO:0000250|UniProtKB:O43324,
CC ECO:0000269|PubMed:12060739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15680327}. Nucleus
CC {ECO:0000269|PubMed:15680327}. Note=Cytoplasmic under growth arrest
CC conditions. Translocated into the nucleus when growth resumes at S
CC phase and following DNA damage.
CC -!- INDUCTION: By DNA damaging agents, such as UV, adriamycin, actinomycin
CC D and cisplatin. {ECO:0000269|PubMed:15680327}.
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DR EMBL; AK003335; BAB22723.1; -; mRNA.
DR EMBL; BC048466; AAH48466.1; -; mRNA.
DR CCDS; CCDS26465.1; -.
DR RefSeq; NP_079656.1; NM_025380.2.
DR AlphaFoldDB; Q9D1M4; -.
DR SMR; Q9D1M4; -.
DR BioGRID; 211246; 10.
DR STRING; 10090.ENSMUSP00000001757; -.
DR MoonProt; Q9D1M4; -.
DR iPTMnet; Q9D1M4; -.
DR PhosphoSitePlus; Q9D1M4; -.
DR EPD; Q9D1M4; -.
DR MaxQB; Q9D1M4; -.
DR PaxDb; Q9D1M4; -.
DR PeptideAtlas; Q9D1M4; -.
DR PRIDE; Q9D1M4; -.
DR ProteomicsDB; 295705; -.
DR DNASU; 66143; -.
DR Ensembl; ENSMUST00000001757; ENSMUSP00000001757; ENSMUSG00000001707.
DR GeneID; 66143; -.
DR KEGG; mmu:66143; -.
DR UCSC; uc007qdw.1; mouse.
DR CTD; 9521; -.
DR MGI; MGI:1913393; Eef1e1.
DR VEuPathDB; HostDB:ENSMUSG00000001707; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00390000003564; -.
DR HOGENOM; CLU_098079_0_0_1; -.
DR InParanoid; Q9D1M4; -.
DR OMA; FIVDLTF; -.
DR OrthoDB; 1422931at2759; -.
DR PhylomeDB; Q9D1M4; -.
DR TreeFam; TF326005; -.
DR BioGRID-ORCS; 66143; 24 hits in 110 CRISPR screens.
DR ChiTaRS; Eef1e1; mouse.
DR PRO; PR:Q9D1M4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D1M4; protein.
DR Bgee; ENSMUSG00000001707; Expressed in embryonic brain and 244 other tissues.
DR Genevisible; Q9D1M4; MM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:2000774; P:positive regulation of cellular senescence; ISO:MGI.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR InterPro; IPR042450; EEF1E1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR PANTHER; PTHR44490; PTHR44490; 1.
DR Pfam; PF00043; GST_C; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Nucleus; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43324"
FT CHAIN 2..174
FT /note="Eukaryotic translation elongation factor 1 epsilon-
FT 1"
FT /id="PRO_0000221133"
FT DOMAIN 50..173
FT /note="GST C-terminal"
FT REGION 2..56
FT /note="N-terminal"
FT /evidence="ECO:0000250"
FT REGION 57..63
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 64..152
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 153..169
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43324"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43324"
SQ SEQUENCE 174 AA; 19859 MW; AC804776D9C0590E CRC64;
MAAAAELRLL EKSLGLKPGN KYSAQGERQI PVLQTNNGPS LMGLSTIATH LVKQASKEHL
LGSTAEEKAM VQQWLEFRVT RVDGHSSKED TQTLLKDLNS YLEDKVYLAG HNITLADILL
YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPDIRQHLS SIVFIKNRLY ANSH
